|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
2-380 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 751.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 2 MIYLDYAATTPMSAEALQTYTKAASQYFGNEQSLHDIGGTASSLLQVCRKTFAEMIGGKEQGIFFTSGGSESNYLAIQSL 81
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 82 LNA--QNKKHIITTPMEHASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAEI 159
Cdd:PRK02948 81 LNAlpQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 160 GALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYINPQVRWTQIFPGTSHEKGFRPGTVNVPG 239
Cdd:PRK02948 161 GALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQVRWKPVFPGTTHEKGFRPGTVNVPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 240 IAAFLTAAENILKNQQEESLRFKGLRSYFLEQIRTLPLKIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRHGIAISTG 319
Cdd:PRK02948 241 IAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPLPIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRRGIAISTG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446896490 320 SACQVGKQEPSKTMLAIGKTYEEAKQYVRFSFGQQTTKDQIDTTIHALHTIGNQFYRGVKS 380
Cdd:PRK02948 321 SACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHALETIGNQFYRGVKI 381
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-370 |
4.45e-175 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 492.26 E-value: 4.45e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 1 MMIYLDYAATTPMSAEALQTYTKAASQYFGNEQSLHDIGGTASSLLQVCRKTFAEMIGGKEQGIFFTSGGSESNYLAIQS 80
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 81 LLNA--QNKKHIITTPMEHASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAE 158
Cdd:COG1104 82 AARAyrKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 159 IGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYINPQVRWTQIFPGTSHEKGFRPGTVNVP 238
Cdd:COG1104 162 IAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 239 GIAAFLTAAENILKNQQEESLRFKGLRSYFLEQIRTLPLKIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRHGIAIST 318
Cdd:COG1104 242 GIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAVSS 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446896490 319 GSACQVGKQEPSKTMLAIGKTYEEAKQYVRFSFGQQTTKDQIDTTIHALHTI 370
Cdd:COG1104 322 GSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEI 373
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
3-370 |
3.09e-121 |
|
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related families of cysteine desulfurase involved in iron-sulfur (FeS) cluster biosynthesis. NifS is part of the NIF system, usually associated with other nif genes involved in nitrogenase expression and nitrogen fixation. The protein family is given a fairly broad interpretation here. It includes a clade nearly always found in extended nitrogen fixation genomic regions, plus a second clade more closely related to the first than to IscS and also part of NifS-like/NifU-like systems. This model does not extend to a more distantly clade found in the epsilon proteobacteria such as Helicobacter pylori, also named NifS in the literature, built instead in TIGR03403.
Pssm-ID: 132443 [Multi-domain] Cd Length: 379 Bit Score: 355.38 E-value: 3.09e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 3 IYLDYAATTPMSAEALQTYTKAASQYFGNEQSLHDIGGTASSLLQVCRKTFAEMIGGKEQGIFFTSGGSESNYLAIQSLL 82
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 83 NAQ-NKKHIITTPMEHASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAEIGA 161
Cdd:TIGR03402 81 AAQpEKRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 162 LLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYINPQVRWTQIFPGTSHEKGFRPGTVNVPGIA 241
Cdd:TIGR03402 161 IAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENVPGIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 242 AFLTAAENILKNQQEESLRFKGLRSYFLEQIRTLPLKIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRHGIAISTGSA 321
Cdd:TIGR03402 241 GLGKAAELATEHLEEENTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICASSGSA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446896490 322 CQVGKQEPSKTMLAIGKTYEEAKQYVRFSFGQQTTKDQIDTTIHALHTI 370
Cdd:TIGR03402 321 CTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPI 369
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
3-361 |
1.14e-81 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 254.09 E-value: 1.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 3 IYLDYAATTPMSAEALQTYTKAASQYFGN-EQSLHDIGGTASSLLQVCRKTFAEMIGGK-EQGIFFTSGGSESNYLAIQS 80
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNvHRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 81 LLNAQNKK-HIITTPMEHASIRSYFQSL-QSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAE 158
Cdd:pfam00266 81 LGRSLKPGdEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 159 IGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYI--NPQVRWTQIFPGTS-------HEKG 229
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGrrDLLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 230 FRP-------GTVNVPGIAAfLTAAENILKNQQEESLRFKG--LRSYFLEQIRTLPLkIEVEGhsTSCLPHIIGVTIKGI 300
Cdd:pfam00266 241 FADapwkfeaGTPNIAGIIG-LGAALEYLSEIGLEAIEKHEheLAQYLYERLLSLPG-IRLYG--PERRASIISFNFKGV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446896490 301 EGQYTMLECNRHGIAISTGSACqvgkQEPSKTMLAIGKTyeeakqyVRFSFGQQTTKDQID 361
Cdd:pfam00266 317 HPHDVATLLDESGIAVRSGHHC----AQPLMVRLGLGGT-------VRASFYIYNTQEDVD 366
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
3-367 |
4.87e-51 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 174.58 E-value: 4.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 3 IYLDYAATTPMSAEALQtytkAASQYFGNEQS-----LHDIGGTASSLLQVCRKTFAEMIGGKEQG-IFFTSGGSESNYL 76
Cdd:cd06453 1 VYLDNAATSQKPQPVID----AIVDYYRHYNAnvhrgVHELSARATDAYEAAREKVARFINAPSPDeIIFTRNTTEAINL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 77 AIQSLLNAQNKK-HIITTPMEHAS-IRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQ 154
Cdd:cd06453 77 VAYGLGRANKPGdEIVTSVMEHHSnIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 155 NIAEIGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYINPQ--------------VRWTQI 220
Cdd:cd06453 157 PVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEElleemppyggggemIEEVSF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 221 FPGTSHEKGFR--PGTVNVPGIAAfLTAA---------ENIlknQQEEslrfKGLRSYFLEQIRTLPlkiEVEGHSTScl 289
Cdd:cd06453 237 EETTYADLPHKfeAGTPNIAGAIG-LGAAidylekigmEAI---AAHE----HELTAYALERLSEIP---GVRVYGDA-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 290 PHIIGV---TIKGIEGQY--TMLecNRHGIAISTGSACqvgkqepskTMLAIGKTYEEAKqyVRFSFGQQTTKDQIDTTI 364
Cdd:cd06453 304 EDRAGVvsfNLEGIHPHDvaTIL--DQYGIAVRAGHHC---------AQPLMRRLGVPGT--VRASFGLYNTEEEIDALV 370
|
...
gi 446896490 365 HAL 367
Cdd:cd06453 371 EAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
90-210 |
4.53e-08 |
|
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.
Pssm-ID: 469077 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 90 IITTPMEH-ASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAEIGALLKKYNV 168
Cdd:NF041166 338 IIVSHLEHhANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGA 417
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446896490 169 LFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACY 210
Cdd:NF041166 418 KVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVY 459
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
2-380 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 751.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 2 MIYLDYAATTPMSAEALQTYTKAASQYFGNEQSLHDIGGTASSLLQVCRKTFAEMIGGKEQGIFFTSGGSESNYLAIQSL 81
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 82 LNA--QNKKHIITTPMEHASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAEI 159
Cdd:PRK02948 81 LNAlpQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 160 GALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYINPQVRWTQIFPGTSHEKGFRPGTVNVPG 239
Cdd:PRK02948 161 GALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQVRWKPVFPGTTHEKGFRPGTVNVPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 240 IAAFLTAAENILKNQQEESLRFKGLRSYFLEQIRTLPLKIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRHGIAISTG 319
Cdd:PRK02948 241 IAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPLPIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRRGIAISTG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446896490 320 SACQVGKQEPSKTMLAIGKTYEEAKQYVRFSFGQQTTKDQIDTTIHALHTIGNQFYRGVKS 380
Cdd:PRK02948 321 SACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHALETIGNQFYRGVKI 381
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-370 |
4.45e-175 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 492.26 E-value: 4.45e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 1 MMIYLDYAATTPMSAEALQTYTKAASQYFGNEQSLHDIGGTASSLLQVCRKTFAEMIGGKEQGIFFTSGGSESNYLAIQS 80
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 81 LLNA--QNKKHIITTPMEHASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAE 158
Cdd:COG1104 82 AARAyrKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 159 IGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYINPQVRWTQIFPGTSHEKGFRPGTVNVP 238
Cdd:COG1104 162 IAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 239 GIAAFLTAAENILKNQQEESLRFKGLRSYFLEQIRTLPLKIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRHGIAIST 318
Cdd:COG1104 242 GIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAVSS 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446896490 319 GSACQVGKQEPSKTMLAIGKTYEEAKQYVRFSFGQQTTKDQIDTTIHALHTI 370
Cdd:COG1104 322 GSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEI 373
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
3-370 |
3.09e-121 |
|
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related families of cysteine desulfurase involved in iron-sulfur (FeS) cluster biosynthesis. NifS is part of the NIF system, usually associated with other nif genes involved in nitrogenase expression and nitrogen fixation. The protein family is given a fairly broad interpretation here. It includes a clade nearly always found in extended nitrogen fixation genomic regions, plus a second clade more closely related to the first than to IscS and also part of NifS-like/NifU-like systems. This model does not extend to a more distantly clade found in the epsilon proteobacteria such as Helicobacter pylori, also named NifS in the literature, built instead in TIGR03403.
Pssm-ID: 132443 [Multi-domain] Cd Length: 379 Bit Score: 355.38 E-value: 3.09e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 3 IYLDYAATTPMSAEALQTYTKAASQYFGNEQSLHDIGGTASSLLQVCRKTFAEMIGGKEQGIFFTSGGSESNYLAIQSLL 82
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 83 NAQ-NKKHIITTPMEHASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAEIGA 161
Cdd:TIGR03402 81 AAQpEKRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 162 LLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYINPQVRWTQIFPGTSHEKGFRPGTVNVPGIA 241
Cdd:TIGR03402 161 IAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENVPGIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 242 AFLTAAENILKNQQEESLRFKGLRSYFLEQIRTLPLKIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRHGIAISTGSA 321
Cdd:TIGR03402 241 GLGKAAELATEHLEEENTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICASSGSA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446896490 322 CQVGKQEPSKTMLAIGKTYEEAKQYVRFSFGQQTTKDQIDTTIHALHTI 370
Cdd:TIGR03402 321 CTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPI 369
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
3-364 |
4.51e-98 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 297.24 E-value: 4.51e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 3 IYLDYAATTPMS---AEALQTYTKAASQyFGNEQSL-HDIGGTASSLLQVCRKTFAEMIGGKEQGIFFTSGGSESNYLAI 78
Cdd:PRK14012 5 IYLDYSATTPVDprvAEKMMPYLTMDGT-FGNPASRsHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 79 QSLLN-AQNK-KHIITTPMEHASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNI 156
Cdd:PRK14012 84 KGAAHfYQKKgKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 157 AEIGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYI--NPQVRWTQIFPGTSHEKGFRPGT 234
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVrrKPRVRLEAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 235 VNVPGIAAFLTAAENILKNQQEESLRFKGLRSYFLEQIRTLPlKIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNrhGI 314
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIE-EVYLNGDLEQRVPGNLNVSFNYVEGESLIMALK--DL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446896490 315 AISTGSACQVGKQEPSKTMLAIGKTYEEAKQYVRFSFGQQTTKDQIDTTI 364
Cdd:PRK14012 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAI 370
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
3-361 |
5.49e-94 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 285.39 E-value: 5.49e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 3 IYLDYAATTPMSAEALQTYTKAASQYFGNEQSL-HDIGGTASSLLQVCRKTFAEMIGGKEQGIFFTSGGSESNYLAIQSL 81
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 82 LNA--QNKKHIITTPMEHASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAEI 159
Cdd:PLN02651 81 MHFykDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 160 GALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYI--NPQVRWTQIFPGTSHEKGFRPGTVNV 237
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVrrRPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 238 PGIAAFLTAAENILKNQQEESLRFKGLRSYFLEQIRTLPLKIEVEGHS--TSCLPHIIGVTIKGIEGQYTMLECNrhGIA 315
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGPRdpEKRYPGTLNLSFAYVEGESLLMGLK--EVA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446896490 316 ISTGSACQVGKQEPSKTMLAIGKTYEEAKQYVRFSFGQQTTKDQID 361
Cdd:PLN02651 319 VSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
4-350 |
1.37e-87 |
|
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a larger family of cysteine desulfurases. It is encoded, typically, divergently from a conserved, sparsely distributed operon for sulfur modification of DNA. This modification system is designated dnd, after the phenotype of DNA degradation during electrophoresis. The system is sporadically distributed in bacteria, much like some restriction enzyme operons. DndB is described as a putative ATPase. [DNA metabolism, Restriction/modification]
Pssm-ID: 163191 [Multi-domain] Cd Length: 353 Bit Score: 268.59 E-value: 1.37e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 4 YLDYAATTPMSAEALQTYTKAASQYFGNEQSL-HDIGGTASSLLQVCRKTFAEMIGGKEQGIFFTSGGSESNYLAIQSLL 82
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRtHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 83 NA---QNKKHIITTPMEHASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAEI 159
Cdd:TIGR03235 81 RAgeqKGKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 160 GALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYIN----PQVRWTQIFPGTSHEKGFRPGTV 235
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRkrgkPKAPLKPIMFGGGQERGLRPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 236 NVPGIAAFLTAAENILKNQQEESLRFKGLRSYFLEQIRTLPlkIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECnRHGIA 315
Cdd:TIGR03235 241 PVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDALQTLG--VKLNGDPAETIPHILNFSIDGVNSEALIVNL-RADAA 317
|
330 340 350
....*....|....*....|....*....|....*
gi 446896490 316 ISTGSACQVGKQEPSKTMLAIGKTYEEAKQYVRFS 350
Cdd:TIGR03235 318 VSTGSACSSSKYEPSHVLQAMGLDTDRARGAIRFS 352
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
3-361 |
1.14e-81 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 254.09 E-value: 1.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 3 IYLDYAATTPMSAEALQTYTKAASQYFGN-EQSLHDIGGTASSLLQVCRKTFAEMIGGK-EQGIFFTSGGSESNYLAIQS 80
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNvHRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 81 LLNAQNKK-HIITTPMEHASIRSYFQSL-QSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAE 158
Cdd:pfam00266 81 LGRSLKPGdEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 159 IGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYI--NPQVRWTQIFPGTS-------HEKG 229
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGrrDLLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 230 FRP-------GTVNVPGIAAfLTAAENILKNQQEESLRFKG--LRSYFLEQIRTLPLkIEVEGhsTSCLPHIIGVTIKGI 300
Cdd:pfam00266 241 FADapwkfeaGTPNIAGIIG-LGAALEYLSEIGLEAIEKHEheLAQYLYERLLSLPG-IRLYG--PERRASIISFNFKGV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446896490 301 EGQYTMLECNRHGIAISTGSACqvgkQEPSKTMLAIGKTyeeakqyVRFSFGQQTTKDQID 361
Cdd:pfam00266 317 HPHDVATLLDESGIAVRSGHHC----AQPLMVRLGLGGT-------VRASFYIYNTQEDVD 366
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
3-370 |
1.25e-53 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 182.26 E-value: 1.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 3 IYLDYAATTPMSAEALQTYTKAASQYFGN-EQSLHDIGGTASSLLQVCRKTFAEMIGGKEQG-IFFTSGGSES-NyLAIQ 79
Cdd:COG0520 17 VYLDNAATGQKPRPVIDAIRDYYEPYNANvHRGAHELSAEATDAYEAAREKVARFIGAASPDeIIFTRGTTEAiN-LVAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 80 SLLNAQNKKHIITTPMEHAS-IRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAE 158
Cdd:COG0520 96 GLGRLKPGDEILITEMEHHSnIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPVKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 159 IGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYINP-----------------QVRWTQIF 221
Cdd:COG0520 176 IAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRellealppflggggmieWVSFDGTT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 222 PGTSHEKgFRPGTVNVPGIAAFLTAA--------ENILKnqqeeslRFKGLRSYFLEQIRTLPlKIEVegHSTSCLPHII 293
Cdd:COG0520 256 YADLPRR-FEAGTPNIAGAIGLGAAIdyleaigmEAIEA-------RERELTAYALEGLAAIP-GVRI--LGPADPEDRS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 294 GV---TIKGIEGQY--TMLecNRHGIAISTGSACqvgkQEPSKTMLAIGKTyeeakqyVRFSFGQQTTKDQIDTTIHALH 368
Cdd:COG0520 325 GIvsfNVDGVHPHDvaALL--DDEGIAVRAGHHC----AQPLMRRLGVPGT-------VRASFHLYNTEEEIDRLVEALK 391
|
..
gi 446896490 369 TI 370
Cdd:COG0520 392 KL 393
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
3-367 |
4.87e-51 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 174.58 E-value: 4.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 3 IYLDYAATTPMSAEALQtytkAASQYFGNEQS-----LHDIGGTASSLLQVCRKTFAEMIGGKEQG-IFFTSGGSESNYL 76
Cdd:cd06453 1 VYLDNAATSQKPQPVID----AIVDYYRHYNAnvhrgVHELSARATDAYEAAREKVARFINAPSPDeIIFTRNTTEAINL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 77 AIQSLLNAQNKK-HIITTPMEHAS-IRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQ 154
Cdd:cd06453 77 VAYGLGRANKPGdEIVTSVMEHHSnIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 155 NIAEIGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYINPQ--------------VRWTQI 220
Cdd:cd06453 157 PVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEElleemppyggggemIEEVSF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 221 FPGTSHEKGFR--PGTVNVPGIAAfLTAA---------ENIlknQQEEslrfKGLRSYFLEQIRTLPlkiEVEGHSTScl 289
Cdd:cd06453 237 EETTYADLPHKfeAGTPNIAGAIG-LGAAidylekigmEAI---AAHE----HELTAYALERLSEIP---GVRVYGDA-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 290 PHIIGV---TIKGIEGQY--TMLecNRHGIAISTGSACqvgkqepskTMLAIGKTYEEAKqyVRFSFGQQTTKDQIDTTI 364
Cdd:cd06453 304 EDRAGVvsfNLEGIHPHDvaTIL--DQYGIAVRAGHHC---------AQPLMRRLGVPGT--VRASFGLYNTEEEIDALV 370
|
...
gi 446896490 365 HAL 367
Cdd:cd06453 371 EAL 373
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
45-212 |
5.21e-19 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 83.59 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 45 LLQVCRKTFAEMIGGKEQGIFFTSGGSESNYLAIQSLLnaQNKKHIITTPMEHASirSYFQSLQSKGYTITEIPVDKN-- 122
Cdd:cd01494 1 KLEELEEKLARLLQPGNDKAVFVPSGTGANEAALLALL--GPGDEVIVDANGHGS--RYWVAAELAGAKPVPVPVDDAgy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 123 GLIRLIDLEE-AITEDTVLASIQHGNSEIGTVQNIAEIGALLKKYNVLFHSDCVQTFG---KLPIHVFEMGIDSLSVSAH 198
Cdd:cd01494 77 GGLDVAILEElKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGaspAPGVLIPEGGADVVTFSLH 156
|
170
....*....|....
gi 446896490 199 KIYGPKGVGACYIN 212
Cdd:cd01494 157 KNLGGEGGGVVIVK 170
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
2-276 |
9.73e-17 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 80.95 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 2 MIYLDYAAttpmSAEALQTYTKAASQYFGNE-----QSLHDIGGTASSLLQVCRKTFAEMIGGK-EQGIFFTSGGSESNY 75
Cdd:PRK09295 24 LAYLDSAA----SAQKPSQVIDAEAEFYRHGyaavhRGIHTLSAQATEKMENVRKQAALFINARsAEELVFVRGTTEGIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 76 LAIQSLLNAQ--NKKHIITTPMEH-ASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGT 152
Cdd:PRK09295 100 LVANSWGNSNvrAGDNIIISEMEHhANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 153 VQNIAEIGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYIN-----------------PQV 215
Cdd:PRK09295 180 ENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKeallqemppwegggsmiATV 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446896490 216 RWTQifpGTSHEKG---FRPGTVNVPGIAAFLTAAE-----NILKNQQEESlrfkGLRSYFLEQIRTLP 276
Cdd:PRK09295 260 SLTE---GTTWAKApwrFEAGTPNTGGIIGLGAALDyvsalGLNNIAEYEQ----NLMHYALSQLESVP 321
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
2-207 |
5.13e-16 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 79.02 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 2 MIYLDYAATT--PMSA-EALQTYTKAasqYFGN-EQSLHDIGGTASSLLQVCRKTFAEMIGGKEQG-IFFTSGGSESNYL 76
Cdd:PLN02855 33 LVYLDNAATSqkPAAVlDALQDYYEE---YNSNvHRGIHALSAKATDAYELARKKVAAFINASTSReIVFTRNATEAINL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 77 AIQS--LLNAQNKKHIITTPMEHASIRSYFQSL-QSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTV 153
Cdd:PLN02855 110 VAYTwgLANLKPGDEVILSVAEHHSNIVPWQLVaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGSI 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446896490 154 QNIAEIGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVG 207
Cdd:PLN02855 190 LPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIG 243
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
9-211 |
6.53e-14 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 439846 [Multi-domain] Cd Length: 460 Bit Score: 72.56 E-value: 6.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 9 ATTPMSAEALQTYTKAASQYFGneqsLHDIGGTASSLLQVCRKTFAEMIGGKEQGI-FFTSGGSESNYLAI----QSLLN 83
Cdd:COG0076 76 GGTTPAALAADLLASALNQNMG----DWDTSPAATELEREVVRWLADLLGLPEGAGgVFTSGGTEANLLALlaarDRALA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 84 AQNKKH---------IITTPMEHASIR---SYFqSLQSKGytITEIPVDKNGLIRLIDLEEAITEDT--------VLASI 143
Cdd:COG0076 152 RRVRAEglpgaprprIVVSEEAHSSVDkaaRLL-GLGRDA--LRKVPVDEDGRMDPDALEAAIDEDRaaglnpiaVVATA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 144 qhGNSEIGTVQNIAEIGALLKKYNVLFHSDCVqtFG-------KLPiHVFEmGI---DSLSVSAHKiYG--PKGVGACYI 211
Cdd:COG0076 229 --GTTNTGAIDPLAEIADIAREHGLWLHVDAA--YGgfalpspELR-HLLD-GIeraDSITVDPHK-WLyvPYGCGAVLV 301
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
3-369 |
1.41e-12 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 68.53 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 3 IYLDYAATtpmsaeAL--QTYTKAASQYFGNEQ-----SLHDIGGTASSLLQVCRKTFAEMIGG-KEQGIFFTSGGSESN 74
Cdd:PRK10874 21 VYLDSAAT------ALkpQAVIEATQQFYSLSAgnvhrSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 75 YLAIQSLLNA--QNKKHIITTPMEH-ASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIG 151
Cdd:PRK10874 95 NLVAQSYARPrlQPGDEIIVSEAEHhANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 152 TVQNIAEIGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACYINPQV-----RW-------TQ 219
Cdd:PRK10874 175 GCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELleamsPWqgggkmlTE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 220 I-FPG-TSHE--KGFRPGTVNVPGIAAF-----------LTAAEN---ILKNQQEESL-RFKGLRSYFLEQIRTLPLKIE 280
Cdd:PRK10874 255 VsFDGfTPQSapWRFEAGTPNVAGVIGLsaalewladidINQAESwsrSLATLAEDALaKLPGFRSFRCQDSSLLAFDFA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 281 VEGHSTSclphiigVTIkgIEGQytmlecnrhGIAISTGSACqvgkQEPSKTMLAIGKTyeeakqyVRFSFGQQTTKDQI 360
Cdd:PRK10874 335 GVHHSDL-------VTL--LAEY---------GIALRAGQHC----AQPLLAALGVTGT-------LRASFAPYNTQSDV 385
|
....*....
gi 446896490 361 DTTIHALHT 369
Cdd:PRK10874 386 DALVNAVDR 394
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
11-209 |
6.96e-12 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 66.07 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 11 TPMSAEALQ----TYTKAASQyFGNEQSlhdiggTASSLL-QVCRKTFAEMIG---GKEQGIFfTSGGSESNYLAiqsLL 82
Cdd:cd06450 7 TTMDPPALLlemlTSAKNAID-FTWDES------PAATEMeAEVVNWLAKLFGlpsEDADGVF-TSGGSESNLLA---LL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 83 NAQNKKH---------------IITTPMEHASIR---SYFQSlqskgyTITEIPVDKNGLIRLIDLEEAITEDT------ 138
Cdd:cd06450 76 AARDRARkrlkagggrgidklvIVCSDQAHVSVEkaaAYLDV------KVRLVPVDEDGRMDPEALEAAIDEDKaeglnp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 139 --VLASIqhGNSEIGTVQNIAEIGALLKKYNVLFHSDCvqTFGKL----PIHVFEM-GI---DSLSVSAHKiYG--PKGV 206
Cdd:cd06450 150 imVVATA--GTTDTGAIDPLEEIADLAEKYDLWLHVDA--AYGGFllpfPEPRHLDfGIervDSISVDPHK-YGlvPLGC 224
|
...
gi 446896490 207 GAC 209
Cdd:cd06450 225 SAV 227
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
129-319 |
1.25e-09 |
|
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 59.33 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 129 DLEEAITED---TVLAsIQHGNSEIGTVQNIAEIGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHK-IYGPK 204
Cdd:COG0075 115 EVEEALAADpdiKAVA-VVHNETSTGVLNPLEEIGALAKEHGALLIVDAVSSLGGVPLDMDEWGIDVVVSGSQKcLMLPP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 205 GVGACYINPQVR--------------WTQIFPgtSHEKGFRPGTVNVPGIAAFLTAAENILknqqEESL-----RFKGLR 265
Cdd:COG0075 194 GLAFVAVSERALeaiearklpsyyldLKLWLK--YWEKGQTPYTPPVSLLYALREALDLIL----EEGLenrfaRHRRLA 267
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446896490 266 SYFLEQIRTLPLKIEVEGHSTSclPHIIGVTI-KGIEGQ--YTMLEcNRHGIAISTG 319
Cdd:COG0075 268 EALRAGLEALGLELFAEEEYRS--PTVTAVRVpEGVDAAalRKRLK-ERYGIEIAGG 321
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
50-368 |
4.66e-09 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 57.35 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 50 RKTFAEMIGG------KEQGIFFTSGGSESNYLAIQSLLNAqNKKHIITTPMeHASIRSYFQSLqskGYTITEIPVDKNG 123
Cdd:cd00609 42 REAIAEWLGRrggvdvPPEEIVVTNGAQEALSLLLRALLNP-GDEVLVPDPT-YPGYEAAARLA---GAEVVPVPLDEEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 124 --LIRLIDLEEAITEDTVLASIQHGNSEIGTV---QNIAEIGALLKKYNVL---------FHSD----CVQTFGKLPIHV 185
Cdd:cd00609 117 gfLLDLELLEAAKTPKTKLLYLNNPNNPTGAVlseEELEELAELAKKHGILiisdeayaeLVYDgeppPALALLDAYERV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 186 FEMGidSLSvsahKIYGPKG--VGACYINPQVRWTQIfpgtshEKGFRPGTVNVPGIAAflTAAENILKNQQEE----SL 259
Cdd:cd00609 197 IVLR--SFS----KTFGLPGlrIGYLIAPPEELLERL------KKLLPYTTSGPSTLSQ--AAAAAALDDGEEHleelRE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 260 RFKGLRSYFLEQIRTLPLKIEVEGHSTSCLphIIGVTIKGIEGQYTMLeCNRHGIAISTGSACqvgkqepsktmlaigkt 339
Cdd:cd00609 263 RYRRRRDALLEALKELGPLVVVKPSGGFFL--WLDLPEGDDEEFLERL-LLEAGVVVRPGSAF----------------- 322
|
330 340
....*....|....*....|....*....
gi 446896490 340 YEEAKQYVRFSFGqqTTKDQIDTTIHALH 368
Cdd:cd00609 323 GEGGEGFVRLSFA--TPEEELEEALERLA 349
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
90-210 |
4.53e-08 |
|
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.
Pssm-ID: 469077 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 90 IITTPMEH-ASIRSYFQSLQSKGYTITEIPVDKNGLIRLIDLEEAITEDTVLASIQHGNSEIGTVQNIAEIGALLKKYNV 168
Cdd:NF041166 338 IIVSHLEHhANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGA 417
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446896490 169 LFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYGPKGVGACY 210
Cdd:NF041166 418 KVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVY 459
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
129-326 |
1.90e-07 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 52.29 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 129 DLEEAITEDTVLA-SIQHGNSEIGTVQNIAEIGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIYG-PKGV 206
Cdd:cd06451 115 EIAEALEQHDIKAvTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGaPPGL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 207 GACYINPQVrWTQIFPGTSH---------------EKGFRPGTVNVPGIAAFLTAAENILknqqEESL-----RFKGLRS 266
Cdd:cd06451 195 GPIAFSERA-LERIKKKTKPkgfyfdlllllkywgEGYSYPHTPPVNLLYALREALDLIL----EEGLenrwaRHRRLAK 269
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446896490 267 YFLEQIRTLPLKIEVEghSTSCLPHIIGVTI-KGIEG----QYTMlecNRHGIAISTGSACQVGK 326
Cdd:cd06451 270 ALREGLEALGLKLLAK--PELRSPTVTAVLVpEGVDGdevvRRLM---KRYNIEIAGGLGPTAGK 329
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
67-206 |
8.56e-06 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 47.34 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 67 TSGGSESNylaIQSLLNAQN--KKHIITTPME-HASIRSYFQSLQSKGYTITEIPvdkNGLIRLIDLEEAITEDTVLASI 143
Cdd:PRK02769 90 TNGGTEGN---LYGCYLARElfPDGTLYYSKDtHYSVSKIARLLRIKSRVITSLP---NGEIDYDDLISKIKENKNQPPI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 144 QHGNseIGT-----VQNIAEIGALLKKY---NVLFHSDCVQTFGKLPI------HVFEMGIDSLSVSAHKIYG---PKGV 206
Cdd:PRK02769 164 IFAN--IGTtmtgaIDNIKEIQEILKKIgidDYYIHADAALSGMILPFvnnpppFSFADGIDSIAISGHKFIGspmPCGI 241
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
42-199 |
2.66e-05 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 45.87 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 42 ASSLLQ-VCRKTFAEMIG------GKEQGIFFTSGGSESNYLAI-------------------QSLLNAqnKKHIITTPM 95
Cdd:pfam00282 76 ACTELEnVVMNWLGEMLGlpaeflGQEGGGVLQPGSSESNLLALlaartkwikrmkaagkpadSSGILA--KLVAYTSDQ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 96 EHASIRSYFQSLqskGYTITEIPVDKNGLIRLIDLEEAITEDT--------VLASIqhGNSEIGTVQNIAEIGALLKKYN 167
Cdd:pfam00282 154 AHSSIEKAALYG---GVKLREIPSDDNGKMRGMDLEKAIEEDKenglipffVVATL--GTTGSGAFDDLQELGDICAKHN 228
|
170 180 190
....*....|....*....|....*....|....*...
gi 446896490 168 VLFHSDCVQTFGKL--PIHVFEM-GI---DSLSVSAHK 199
Cdd:pfam00282 229 LWLHVDAAYGGSAFicPEFRHWLfGIeraDSITFNPHK 266
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
51-209 |
7.11e-05 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 44.25 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 51 KTFAEMIGgKEQGiFFTSGGSESNYLAIQSLLN------AQNKKHIITTpmEHASIrSYFQSLQSkgytiteIPVD-KNG 123
Cdd:cd06502 39 ARAAELFG-KEAA-LFVPSGTAANQLALAAHTQpggsviCHETAHIYTD--EAGAP-EFLSGVKL-------LPVPgENG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 124 LIRLIDLEEAITED-------TVLASIQ--HGNSEIGTVQNIAEIGALLKKYNVLFHSDCVQ-----TFGKLPIHVFEMG 189
Cdd:cd06502 107 KLTPEDLEAAIRPRddihfppPSLVSLEntTEGGTVYPLDELKAISALAKENGLPLHLDGARlanaaAALGVALKTYKSG 186
|
170 180
....*....|....*....|
gi 446896490 190 IDSLSVSahkiyGPKGVGAC 209
Cdd:cd06502 187 VDSVSFC-----LSKGGGAP 201
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
36-199 |
3.75e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 41.82 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 36 HDIGGTASSLLQVCrKTFAEMIGgKEQGIFFTSGgSESNYLAIQSLLnaQNKKHIITTpmEHASIrsYF------QSLQs 109
Cdd:pfam01212 25 DEVYGGDPTVNRLE-DRVAELFG-KEAALFVPSG-TAANQLALMAHC--QRGDEVICG--EPAHI--HFdetgghAELG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 110 kGYTITEIPVDKNGLIRLIDLEEAITED-------TVLASI-QHGNSEIGTV---QNIAEIGALLKKYNVLFHSD----- 173
Cdd:pfam01212 95 -GVQPRPLDGDEAGNMDLEDLEAAIREVgadifppTGLISLeNTHNSAGGQVvslENLREIAALAREHGIPVHLDgarfa 173
|
170 180 190
....*....|....*....|....*....|
gi 446896490 174 --CVqtfgKLPIHVFEM--GIDSLSVSAHK 199
Cdd:pfam01212 174 naAV----ALGVIVKEItsYADSVTMCLSK 199
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
100-170 |
8.62e-04 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 41.28 E-value: 8.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446896490 100 IRSYfqsLQSKGYTITEIPVDkNGLIRLIDLEEAITEDTVLASIQHGNSeIGTVQNIAEIGALLKKYNVLF 170
Cdd:PRK00451 171 LKTY---LKGQGIEVVEVPYE-DGVTDLEALEAAVDDDTAAVVVQYPNF-FGVIEDLEEIAEIAHAGGALF 236
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
66-206 |
3.97e-03 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 39.14 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 66 FTSGGSESNYLAIQSLLNAqnKKHIITTPMEHASirSYFqSLQSKGYTITEIPVDKNGLIRlIDLE------EAITEDT- 138
Cdd:PRK09331 83 VTHGAREGKFAVMHSLCKK--GDYVVLDGLAHYT--SYV-AAERAGLNVREVPKTGYPEYK-ITPEayaekiEEVKEETg 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446896490 139 ---VLASIQHGNSEIGTVQNIAEIGALLKKYNVLFHSDCVQTFGKLPIHVFEMGIDSLSVSAHKIY---GPKGV 206
Cdd:PRK09331 157 kppALALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSGHKSMaasAPSGV 230
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
100-170 |
4.52e-03 |
|
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440172 [Multi-domain] Cd Length: 442 Bit Score: 38.86 E-value: 4.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446896490 100 IRSYFQSLqskGYTITEIPvDKNGLIRLIDLEEAITEDTVLASIQHGNSEiGTVQNIAEIGALLKKYNVLF 170
Cdd:COG0403 172 LKTYAEPL---GIEVVEVP-DEDGVTDLEALKALLDDDVAGVLVQYPNFF-GVIEDLRAIAEAAHAAGALV 237
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
115-207 |
8.55e-03 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 37.97 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896490 115 TEIPVDKNGLIRLIDLEEAITEDtvlASIQH---GNSEIGT-VQN-IAEIGALLKKYNVLFHSDCVQTFGKLPIHVFEMG 189
Cdd:PRK13479 107 VVLDTGEDEPPDAAEVEAALAAD---PRITHvalVHCETTTgILNpLDEIAAVAKRHGKRLIVDAMSSFGAIPIDIAELG 183
|
90
....*....|....*....
gi 446896490 190 IDSLSVSAHK-IYGPKGVG 207
Cdd:PRK13479 184 IDALISSANKcIEGVPGFG 202
|
|
| |
